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• W2565032214 abstract "a) two readily accessible, r eacting with iodoacetate without reduction in the activity of the enzyme; b) two completely masked, accessible to reagents only after the denaturation of the protein; and c) one partial masked, functionally important, and apparently located in the region of the active center of the enzyme. The last-mentioned group is inaccessible to alkylating reagents in the absence of substrates, but can be blocked by p-mercuribenzoat e at pH 4.6 [3]. In the presence of an amino and keto substrate, i.e., during the action of the enzyme, it is subjected to syncatalytic modification of N-ethylmaleimide or 5,5'-dithiobis(2 -nitrobenzoate) with 95% suppression of the enzyme activity [5, 6]. We [7], and also Birchmeier et al., [6] have found that this SH group belongs to the cysteine residue occupying position 390 in the peptide chain of the enzyme. The present paper gives the results of the identification of the readily accessible and the completely masked SH groups of aspartate transaminase from pig-heart cytosol. The readily accessible cysteine residues were labelled in the native enzyme by alkylation with [14C] iodoacetic acid. Then the protein was digested with trypsin and the hydrolyzate was investigated by paper electrophoresis at pH 6.5. The electrophoretogr am showed two radioactive bands: a band coinciding in mobility with neutral amino acids and a band migrating on electrophoresis in the direction towards the anode. Both bands were cut out, stitched to new sheets of paper, and chromatographed. The radioautograms of the peptide map showed that each of the bands contained one radioactive peptide. The Rf values of these peptides were ~ 0.19 and ~ 0.35. Then the peptides were purified by electrophoresis at pH 3°5 and by rechromatography . The peptide with neutral properties (less mobile on chromatography) contained threonine at the N end and arginine at the C end. An amino-acid analysis of an acid hydrolyzate of this peptide showed the presence of the following amino acids (gmole): Cys(CM) 0.017, Thr 0.019, Ser 0.025, Ala 0.026, Arg 0.023, and traces of Gly. Thus, the peptide may be shown in the form Thr[Cys(CM), Ala, Ser]Arg. On comparing the structure of the peptide with the primary structure of the transaminase, it can be seen that we had isolated the peptide 81-85 including the Cys-82 residue. The peptide with more acidic properties also had threonine at the N end and arginine at the C end. The N-terminal segment of the peptide had the sequence Thr-Asp-Asp. The composition of this peptide was determined by the quantitative dansyl method;* in addition to those already mentioned, the amino acids Cys(CM), Glu, Pro, Val, and Leu were found. Consequently, the peptide can be represented in the form:" @default.
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• W2565032214 date "1974-01-01" @default.
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• W2565032214 title "TRANSAMINASE F ROM P IG-HEART C YTOSOL" @default.
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